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Makhnevych, T.* ; Wong, P. ; Pogoutse, O.* ; Vizeacoumar, F.J.* ; Greenblatt, J.F.* ; Emili, A.* ; Houry, W.A.*

Hsp110 is required for spindle length control.

J. Cell Biol. 198, 623-636 (2012)
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Systematic affinity purification combined with mass spectrometry analysis of N- and C-tagged cytoplasmic Hsp70/Hsp110 chaperones was used to identify new roles of Hsp70/Hsp110 in the cell. This allowed the mapping of a chaperone-protein network consisting of 1,227 unique interactions between the 9 chaperones and 473 proteins and highlighted roles for Hsp70/Hsp110 in 14 broad biological processes. Using this information, we uncovered an essential role for Hsp110 in spindle assembly and, more specifically, in modulating the activity of the widely conserved kinesin-5 motor Cin8. The role of Hsp110 Sse1 as a nucleotide exchange factor for the Hsp70 chaperones Ssa1/Ssa2 was found to be required for maintaining the proper distribution of kinesin-5 motors within the spindle, which was subsequently required for bipolar spindle assembly in S phase. These data suggest a model whereby the Hsp70-Hsp110 chaperone complex antagonizes Cin8 plus-end motility and prevents premature spindle elongation in S phase.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Anaphase-Promoting Complex; Saccharomyces-Cerevisiae; Budding Yeast; Protein Complexes; Mitotic Spindle; Dna-Replication; Exchange Factor; Hsp70 Family; Chaperone; Cell
Language english
Publication Year 2012
HGF-reported in Year 2012
ISSN (print) / ISBN 0021-9525
e-ISSN 1540-8140
Journal Journal of Cell Biology, The
Quellenangaben Volume: 198, Issue: 4, Pages: 623-636 Article Number: , Supplement: ,
Publisher Rockefeller University Press
Reviewing status Peer reviewed
Institute(s) Institute of Bioinformatics and Systems Biology (IBIS)
POF-Topic(s) 30505 - New Technologies for Biomedical Discoveries
Research field(s) Enabling and Novel Technologies
PSP Element(s) G-503700-001
PubMed ID 22908312
DOI 10.1083/jcb.201111105
WOS ID WOS:000307932200014
Scopus ID 84866395411
Erfassungsdatum 2012-09-27
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